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Related Experiment Videos

Carboxypeptidase Y stability.

W S Lewis1, S M Schuster

  • 1Department of Chemistry, University of Nebraska-Lincoln 68588-0304.

The Journal of Biological Chemistry
|November 5, 1991
PubMed
Summary
This summary is machine-generated.

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Carboxypeptidase Y stability varies with conditions. High temperatures and pH denature the enzyme, while some solvents and detergents differentially affect its hydrolysis and transpeptidation activities, impacting protein labeling.

Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • Carboxypeptidase Y is a key enzyme in protein and peptide modification.
  • Understanding its stability is crucial for applications like protein labeling.

Purpose of the Study:

  • To investigate the stability of carboxypeptidase Y under various conditions.
  • To determine the impact of cosolvents and detergents on enzyme activity.

Main Methods:

  • Enzyme activity assays for hydrolysis and transpeptidation.
  • Incubation of carboxypeptidase Y under varying pH, temperature, and solvent conditions.

Main Results:

  • High temperature and pH rapidly abolished both enzyme activities.
  • Ammonium sulfate selectively reduced transpeptidation activity.

Related Experiment Videos

  • Organic solvents and Triton X-100 differentially affected hydrolysis and transpeptidation, with some solvents completely inactivating the enzyme.
  • Sodium dodecyl sulfate preferentially reduced hydrolysis activity over transpeptidation.

    • Conclusions:

    • Carboxypeptidase Y exhibits differential stability depending on the chemical environment.
    • The selective loss of activities has significant implications for using the enzyme in peptide and protein labeling techniques.